期刊
CELL REPORTS
卷 18, 期 9, 页码 2175-2188出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.02.003
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资金
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- NIH, NIAID, Division of AIDS Simian Vaccine Evaluation Unit program support under Advanced BioScience Laboratories SVEU [N01-AI-60005]
- NIAID [R01-AI120801]
- Medical Scientist Training Program (MSTP) [T32GM007171]
- Ruth L. Kirschstein National Research Service [F30AI122982-0]
- T32 AIDS Training Grant [AI007392]
- NIH, NIAID, Division of AIDS UM1 grant [AI100645]
- NIAID
Induction of broadly neutralizing antibodies (bnAbs) that target HIV-1 envelope (Env) is a goal of HIV-1 vaccine development. A bnAb target is the Env third variable loop (V3)-glycan site. To determine whether immunization could induce antibodies to the V3-glycan bnAb binding site, we repetitively immunized macaques over a 4-year period with an Env expressing V3-high mannose glycans. Env immunizations elicited plasma antibodies that neutralized HIV-1 expressing only high-mannose glycans-a characteristic shared by early bnAb B cell lineage members. A rhesus recombinant monoclonal antibody from a vaccinated macaque bound to the V3-glycan site at the same amino acids as broadly neutralizing antibodies. A structure of the antibody bound to glycan revealed that the three variable heavy-chain complementarity-determining regions formed a cavity into which glycan could insert and neutralized multiple HIV-1 isolates with high-mannose glycans. Thus, HIV-1 Env vaccination induced mannose-dependent antibodies with characteristics of V3-glycan bnAb precursors.
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